Source:http://linkedlifedata.com/resource/pubmed/id/12029160
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
Pt 6
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pubmed:dateCreated |
2002-5-24
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pubmed:abstractText |
Human respiratory syncytial virus (HRSV) escape mutants selected with antibodies specific for the attachment (G) protein contain diverse genetic alterations, including point mutations, premature stop codons, frame shift changes and A to G hypermutations. The latter changes have only been found in mutants selected with antibodies directed against the conserved central region of the G protein. This gene segment fulfils substrate requirements for adenosine deaminases that act on RNA (ADARs): i.e. it is an A+U rich region of 137 residues, and 98 or 106 of them--for A/Mon/3/88 or Long HRSV strains, respectively--are predicted to form intramolecular base pairs leading to a stable RNA secondary structure. In addition, when sequences of the G gene from natural isolates are compared in terms of pairwise substitutions, A to G+G to A changes are preferentially observed in regions where stable intramolecular dsRNA secondary structures are predicted to occur. In this study, a model is proposed in which, in addition to nucleotide misincorporations, reiterative A to G changes in HRSV are generated by ADAR activity operating in short segments (100-200 ribonucleotide residues) of the HRSV genome with high tendency for intramolecular base pairing.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenine,
http://linkedlifedata.com/resource/pubmed/chemical/Adenosine Deaminase,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Monoclonal,
http://linkedlifedata.com/resource/pubmed/chemical/Antibodies, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine,
http://linkedlifedata.com/resource/pubmed/chemical/HN Protein,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Viral,
http://linkedlifedata.com/resource/pubmed/chemical/Viral Envelope Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/attachment protein G
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0022-1317
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
83
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1445-55
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12029160-Adenine,
pubmed-meshheading:12029160-Adenosine Deaminase,
pubmed-meshheading:12029160-Antibodies, Monoclonal,
pubmed-meshheading:12029160-Antibodies, Viral,
pubmed-meshheading:12029160-Base Sequence,
pubmed-meshheading:12029160-Genome, Viral,
pubmed-meshheading:12029160-Guanine,
pubmed-meshheading:12029160-HN Protein,
pubmed-meshheading:12029160-Models, Genetic,
pubmed-meshheading:12029160-Molecular Sequence Data,
pubmed-meshheading:12029160-Nucleic Acid Conformation,
pubmed-meshheading:12029160-Point Mutation,
pubmed-meshheading:12029160-RNA, Viral,
pubmed-meshheading:12029160-Respiratory Syncytial Virus, Human,
pubmed-meshheading:12029160-Viral Envelope Proteins
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pubmed:year |
2002
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pubmed:articleTitle |
A model for the generation of multiple A to G transitions in the human respiratory syncytial virus genome: predicted RNA secondary structures as substrates for adenosine deaminases that act on RNA.
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pubmed:affiliation |
Centro Nacional de Biología Fundamental, Instituto de Salud Carlos III, Majadahonda, 28220 Madrid, Spain.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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